Reactome | SUMOylation of PCNA with SUMO1

SUMOylation of PCNA with SUMO1

Stable Identifier

R-HSA-4615910

Type

Reaction [transition]

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

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PCNA is SUMOylated with SUMO1 at lysine-164, lysine-254, and other residues (Papouli et al. 2005, Pfander et al. 2005, Gali et al. 2012, Impens et al. 2014). SUMO1 is predominant in vivo. SUMOylation prevents double strand break formation and recombination if DNA replication stalls at lesions (Gali et al. 2012). This is comparable to the situation in Saccharomyces cerevisiae where sumoylated PCNA recruits the Srs2 helicase to prevent recombination during S phase (Pfander et al. 2005, Papouli et al. 2005). In the yeast PCNA homolog, SUMO at lysine-164 is located on the opposite face of PCNA from the face that interacts with DNA polymerase (Freudenthal et al. 2011).

Literature References

PubMed ID	Title	Journal	Year
22457066	Role of SUMO modification of human PCNA at stalled replication fork Gali, H, Juhasz, S, Morocz, M, Hajdu, I, Fatyol, K, Szukacsov, V, Burkovics, P, Haracska, L	Nucleic Acids Res.	2012
21167178	Crystal structure of SUMO-modified proliferating cell nuclear antigen Freudenthal, BD, Brogie, JE, Gakhar, L, Kondratick, CM, Washington, MT	J. Mol. Biol.	2011
15989970	Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p Papouli, E, Chen, S, Davies, AA, Huttner, D, Krejci, L, Sung, P, Ulrich, HD	Mol. Cell	2005
15931174	SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase Pfander, B, Moldovan, GL, Sacher, M, Hoege, C, Jentsch, S	Nature	2005
25114211	Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli Impens, F, Radoshevich, L, Cossart, P, Ribet, D	Proc. Natl. Acad. Sci. U.S.A.	2014